Research workbench
Human NUDT22
Analyse Human NUDT22 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LOR
- Type
- protein
- Length
- 581 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoside diphosphate-linked moiety X motif 22
- UniProt
- Q9BRQ3
- Ligands
- UPG
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoside diphosphate-linked moiety X motif 22 | protein | 290 | 37% helix, 26% strand | Q9BRQ3 |
| B | Nucleoside diphosphate-linked moiety X motif 22 | protein | 291 | 31% helix, 27% strand | Q9BRQ3 |
Ligands and binding sites
- UPG · Uridine-5'-diphosphate-glucose · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 654 | 0.79 | 0.84 | 67 | UPG |
| 2 | 508 | 0.70 | 0.80 | 49 | empty |
| 3 | 80 | 0.45 | 0.81 | 18 | empty |
| 4 | 71 | 0.34 | 0.76 | 12 | empty |
| 5 | 51 | 0.25 | 0.73 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 690 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9BRQ3
- Elsewhere: RCSB PDB 5LOR · PDBe 5LOR · UniProt Q9BRQ3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.